Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.
Journal
The Plant cell
ISSN: 1532-298X
Titre abrégé: Plant Cell
Pays: England
ID NLM: 9208688
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
received:
20
04
2020
revised:
11
08
2020
accepted:
21
10
2020
pubmed:
24
10
2020
medline:
13
4
2021
entrez:
23
10
2020
Statut:
ppublish
Résumé
Posttranslational protein targeting requires chaperone assistance to direct insertion-competent proteins to integration pathways. Chloroplasts integrate nearly all thylakoid transmembrane proteins posttranslationally, but mechanisms in the stroma that assist their insertion remain largely undefined. Here, we investigated how the chloroplast chaperonin (Cpn60) facilitated the thylakoid integration of Plastidic type I signal peptidase 1 (Plsp1) using in vitro targeting assays. Cpn60 bound Plsp1 in the stroma. In isolated chloroplasts, the membrane integration of imported Plsp1 correlated with its dissociation from Cpn60. When the Plsp1 residues that interacted with Cpn60 were removed, Plsp1 did not integrate into the membrane. These results suggested Cpn60 was an intermediate in thylakoid targeting of Plsp1. In isolated thylakoids, the integration of Plsp1 decreased when Cpn60 was present in excess of cpSecA1, the stromal motor of the cpSec1 translocon that inserts unfolded Plsp1 into the thylakoid. An excess of cpSecA1 favored integration. Introducing Cpn60's obligate substrate RbcL displaced Cpn60-bound Plsp1; then, the released Plsp1 exhibited increased accessibility to cpSec1. These in vitro targeting experiments support a model in which Cpn60 captures and then releases insertion-competent Plsp1, whereas cpSecA1 recognizes free Plsp1 for integration. Thylakoid transmembrane proteins in the stroma can interact with Cpn60 to shield themselves from the aqueous environment.
Identifiants
pubmed: 33093145
pii: tpc.20.00309
doi: 10.1105/tpc.20.00309
pmc: PMC7721336
doi:
Substances chimiques
Membrane Proteins
0
Molecular Chaperones
0
Thylakoid Membrane Proteins
0
Serine Endopeptidases
EC 3.4.21.-
type I signal peptidase
EC 3.4.21.89
Chaperonins
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3884-3901Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2020 American Society of Plant Biologists. All rights reserved.
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